TAILIEUCHUNG - Báo cáo khoa học: Folding and turnover of human iron regulatory protein 1 depend on its subcellular localization

Aconitases are iron–sulfur hydrolyases catalysing the interconversion of cit-rate and isocitrate in a wide variety of organisms. Eukaryotic aconitases have been assigned additional roles, as in the case of the metazoan dual activity cytosolic aconitase–iron regulatory protein 1 (IRP1). This human protein was produced in yeast mitochondria to probe IRP1 folding in this organelle where iron–sulfur synthesis originates. | ỊFEBS Journal Folding and turnover of human iron regulatory protein 1 depend on its subcellular localization Alain Martelli1 Benedicts Salin2 Camille Dycke1 Mathilde Louwagie3 Jean-Pierre Andrieu4 Pierre Richaud5 and Jean-Marc Moulis1 1 Laboratoire de Biophysique Moleculaire et Cellulaire UMR-CNRS 5090 Universite Joseph Fourier CEA-Grenoble France 2 Institut de Biochimie et Genetique Cellulaires du Centre Nationalde la Recherche Scientifique UMR-CNRS 5095 Universite Victor Segalen Bordeaux France 3 Laboratoire de Chimie des Proteines ERIT-M 02-01 CEA-Grenoble France 4 Institut de Biologie Structurale JP Ebel CEA CNRS Universite Joseph Fourier Grenoble France 5 Laboratoire des Echanges Membranaires et Signalization UMR-CNRS 6191 Aix-Marseille II Saint Paulles Durance France Keywords aggregation iron-sulfur cluster biogenesis a-ketoglutarate dehydrogenase Saccharomyces cerevisiae translocation Correspondence . Moulis CEA-Grenoble DRDC BMC 17 rue des Martyrs 38054 Grenoble Cedex 9 France Tel 33 4 38 78 56 23 E-mail Received 24 October 2006 revised 4 December 2006 accepted 19 December 2006 doi Aconitases are iron-sulfur hydrolyases catalysing the interconversion of citrate and isocitrate in a wide variety of organisms. Eukaryotic aconitases have been assigned additional roles as in the case of the metazoan dual activity cytosolic aconitase-iron regulatory protein 1 IRP1 . This human protein was produced in yeast mitochondria to probe IRP1 folding in this organelle where iron-sulfur synthesis originates. The behaviour of human IRP1 was compared with that of genuine mitochondrial yeast or human aconitases. All enzymes were functional in yeast mitochondria but IRP1 was found to form dense particles as detected by electron microscopy. MS analysis of purified inclusion bodies evidenced the presence of human IRP1 and a-ketoglutarate dehydrogenase complex component 1 KGD1 one of the subunits of a-ketoglutarate .

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